FUT8 Alpha-(1,6)-Fucosyltransferase in Cancer

Bastian, Kayla; Scott, Emma; Elliott, David; Munkley, Jennifer

doi:10.3390/ijms22010455

Cited by 102 publications

(70 citation statements)

References 151 publications

(160 reference statements)

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“…Accumulating studies have demonstrated that tumorigenesis and development are closely related to the abnormal expression of GTs ( Meech et al, 2019 ; Akella et al, 2020 ; Bastian et al, 2021 ). C1GALT1 is one of the important members of the GT family.…”

Section: Discussionmentioning

confidence: 99%

C1GALT1, Negatively Regulated by miR-181d-5p, Promotes Tumor Progression via Upregulating RAC1 in Lung Adenocarcinoma

Xiao

Liu

Deng

et al. 2021

Front. Cell Dev. Biol.

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Glycosyltransferases are frequently dysregulated in lung cancer. Core 1 β 1, 3-galactosyltransferase 1 (C1GALT1), an enzyme highly expressed in various cancers, is correlated with tumor initiation and development. However, the role of C1GALT1 in lung cancer remains poorly understood. In this study, through bioinformatic analysis and clinical validation, we first discovered that C1GALT1 expression was upregulated in lung adenocarcinoma (LUAD) tissues and was closely related to poor prognosis in patients with LUAD. Gain- and loss-of-function experiments showed that C1GALT1 promoted LUAD cell proliferation, migration, and invasion in vitro, as well as tumor formation in vivo. Further investigation demonstrated that RAC1 expression was positively regulated by C1GALT1 in LUAD, whereas silencing Rac1 could reverse C1GALT1-induced tumor growth and metastasis. Moreover, miR-181d-5p was identified as a negative regulator for C1GALT1 in LUAD. As expected, the inhibitory effects of miR-181d-5p on LUAD cell proliferation, migration, and invasion were counteracted by restoration of C1GALT1. In summary, our results highlight the importance of the miR-181d-5p/C1GALT1/RAC1 regulatory axis during LUAD progression. Thus, C1GALT1 may serve as a potential therapeutic target for LUAD.

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Section: Discussionmentioning

confidence: 99%

C1GALT1, Negatively Regulated by miR-181d-5p, Promotes Tumor Progression via Upregulating RAC1 in Lung Adenocarcinoma

Xiao

Liu

Deng

et al. 2021

Front. Cell Dev. Biol.

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“…Using PC3 and LNCaP cells as models, they also confirmed that FUT8 overexpression in LNCaP cells increased PCa cell migration, while the silencing of FUT8 expression in PC3 cells reduced cell motility. These results suggest the association of FUT8 with aggressive prostate cancer (Table 2) [91,101].…”

Section: Fucosylated N-glycansmentioning

confidence: 63%

“…Core fucosylation transforms cell surface molecules as well as the tumor microenvironment, and thus the extracellular matrix and growth factors, supporting cancer progression. FUT8 promotes cancer cell invasiveness by remodelling the core fucosylation of the TGF-β receptor [88,89], as the presence of core fucose strongly affects the binding affinity of the TGF-β receptor and thus TGF-β induced epithelial-mesenchymal transformation (EMT) [90,91].…”

Section: Fucosylated N-glycansmentioning

confidence: 99%

“…Lange et al reported that β1,6-GlcNAc tri-and tetra-branched N-glycans were increased in cell line xenograft mouse models of prostate cancer (Table 2) [97]. Additionally, it was found that patients with castration-resistant prostate cancer had both overexpressed transcription levels of N-glycan branching enzymes and increased tri-and tetra-antennary N-glycans [91,96]. Slightly different observations were reported for direct expressed-prostatic secretion (EPS) and EPS urine samples.…”

Section: Branched N-glycansmentioning

confidence: 99%

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Glycosylation: Rising Potential for Prostate Cancer Evaluation

Kałuża

Szczykutowicz

Ferens-Sieczkowska

2021

Cancers

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Prostate cancer is the second most commonly diagnosed cancer among men. Alterations in protein glycosylation are confirmed to be a reliable hallmark of cancer. Prostate-specific antigen is the biomarker that is used most frequently for prostate cancer detection, although its lack of sensitivity and specificity results in many unnecessary biopsies. A wide range of glycosylation alterations in prostate cancer cells, including increased sialylation and fucosylation, can modify protein function and play a crucial role in many important biological processes in cancer, including cell signalling, adhesion, migration, and cellular metabolism. In this review, we summarize studies evaluating the prostate cancer associated glycosylation related alterations in sialylation, mainly α2,3-sialylation, core fucosylation, branched N-glycans, LacdiNAc group and presence of truncated O-glycans (sTn, sT antigen). Finally, we discuss the great potential to make use of glycans as diagnostic and prognostic biomarkers for prostate cancer.

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“…Alterations in the addition of fucose to precursor glycan structures promote cell proliferation, migration, adhesion to extracellular matrix, invasiveness, metastasis, maintenance of CSCs, TGF-β-induced EMT and multidrug-resistance (MDR) [ 40 , 41 , 42 , 43 , 44 , 45 ]. Oligosaccharides are fucosylated by FUTs in order to synthesize Lewis antigens, which are involved in cell adhesion to endothelial cells, tumor metastasis, tissue differentiation and inflammation.…”

Section: Glycosyltransferase Gene Expression Profile In Colorectal Cancermentioning

confidence: 99%

The Role of Glycosyltransferases in Colorectal Cancer

Fernández-Ponce

Geribaldi-Doldán

Sánchez-Gomar

et al. 2021

IJMS

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Colorectal cancer (CRC) is one of the main causes of cancer death in the world. Post-translational modifications (PTMs) have been extensively studied in malignancies due to its relevance in tumor pathogenesis and therapy. This review is focused on the dysregulation of glycosyltransferase expression in CRC and its impact in cell function and in several biological pathways associated with CRC pathogenesis, prognosis and therapeutic approaches. Glycan structures act as interface molecules between cells and their environment and in several cases facilitate molecule function. CRC tissue shows alterations in glycan structures decorating molecules, such as annexin-1, mucins, heat shock protein 90 (Hsp90), β1 integrin, carcinoembryonic antigen (CEA), epidermal growth factor receptor (EGFR), insulin-like growth factor-binding protein 3 (IGFBP3), transforming growth factor beta (TGF-β) receptors, Fas (CD95), PD-L1, decorin, sorbin and SH3 domain-containing protein 1 (SORBS1), CD147 and glycosphingolipids. All of these are described as key molecules in oncogenesis and metastasis. Therefore, glycosylation in CRC can affect cell migration, cell–cell adhesion, actin polymerization, mitosis, cell membrane repair, apoptosis, cell differentiation, stemness regulation, intestinal mucosal barrier integrity, immune system regulation, T cell polarization and gut microbiota composition; all such functions are associated with the prognosis and evolution of the disease. According to these findings, multiple strategies have been evaluated to alter oligosaccharide processing and to modify glycoconjugate structures in order to control CRC progression and prevent metastasis. Additionally, immunotherapy approaches have contemplated the use of neo-antigens, generated by altered glycosylation, as targets for tumor-specific T cells or engineered CAR (Chimeric antigen receptors) T cells.

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FUT8 Alpha-(1,6)-Fucosyltransferase in Cancer

Cited by 102 publications

References 151 publications

C1GALT1, Negatively Regulated by miR-181d-5p, Promotes Tumor Progression via Upregulating RAC1 in Lung Adenocarcinoma

C1GALT1, Negatively Regulated by miR-181d-5p, Promotes Tumor Progression via Upregulating RAC1 in Lung Adenocarcinoma

Glycosylation: Rising Potential for Prostate Cancer Evaluation

The Role of Glycosyltransferases in Colorectal Cancer

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